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</script>pmid: 5135502
Abstract In the synthesis of phosphatidic acid catalyzed by a particulate fraction from Clostridium butyricum in the presence of fatty acyl derivatives of an acyl carrier protein (ACP) and sn -glycero-3-phosphate, the first acylation of glycero-3-P is more rapid with an unsaturated acyl-ACP than with a saturated acyl-ACP. In the phosphatidic acid formed, carbon-1 is preferentially acylated with an unsaturated fatty acid and carbon-2 with a saturated fatty acid, as they are in the cellular phospholipids. Acylation by the saturated fatty acid at C2 is not very specific for the acyl carrier: palmityl-CoA competes effectively with palmityl-ACP.
Clostridium, Carbon Isotopes, Acylation, Fatty Acids, Oleic Acids, Palmitic Acids, Tritium, Bacterial Proteins, Glycerophosphates, Coenzyme A, Carrier Proteins, Phospholipids, Protein Binding
Clostridium, Carbon Isotopes, Acylation, Fatty Acids, Oleic Acids, Palmitic Acids, Tritium, Bacterial Proteins, Glycerophosphates, Coenzyme A, Carrier Proteins, Phospholipids, Protein Binding
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| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Average |
